Zobrazeno 1 - 10
of 12
pro vyhledávání: '"Octaaf J.M. Bos"'
Autor:
Marcel J.E. Fischer, Jaap Wilting, Fred R. Opperdoes, Isabelle Coppens, Eugene L.M. Vansterkenburg, Lambert H.M. Janssen, Octaaf J.M. Bos
Publikováno v:
Acta Tropica. 54:237-250
In plasma, a significant part of suramin circulates in tight association with low-density lipoproteins (LDL). At therapeutically obtainable concentrations (100 microM) of suramin, about 85% of the total amount of the drug was bound to proteins, appro
Autor:
Jaap Wilting, RenéF. van der Linden, Lambert H.M. Janssen, Octaaf J.M. Bos, Marcel J.E. Fischer
Publikováno v:
Biochemical Pharmacology. 45:2411-2416
The binding properties of the steroids testosterone and pregnenolone to human serum albumin (HSA) and derived fragments of albumin have been investigated by means of equilibrium dialysis and circular dichroism. The 46 kDa peptic fragment (P46) of HSA
Autor:
Marcel J.E. Fischer, Rene F. van der Linden, Lambert H.M. Janssen, Roel Melsert, Octaaf J.M. Bos, Jos W. Hoogerbrugge, Jaap Wilting, Focko F. G. Rommerts
Publikováno v:
Molecular and Cellular Endocrinology. 82:23-32
__Abstract__ The effects of purified albumin species and albumin fragments (0.2–1% w/v) on short-term (4 h) steroid secretion by immature rat Leydig cells, in the presence of a maximally stimulating dose of luteinizing hormone (LH), were investigat
Autor:
Jan Paul C.I. Boon, Jaap Wilting, Octaaf J.M. Bos, Lambert H.M. Janssen, Marcel J.E. Fischer, Eugene L.M. Vansterkenburg
Publikováno v:
Biochemical pharmacology. 40(7)
The objective of the present study was to investigate the location of the high-affinity suramin binding sites on the human serum albumin molecule. For this purpose, circular dichroism and equilibrium dialysis experiments were performed on the interac
Autor:
D. A. H. v. Maarschalkerwaart, N. Auzeil, L. Christiaens, H. Robaux, D. Schols, A. M. Ouero, Marcel J.E. Fischer, P. Wigerinck, P. Herdewiin, R. Bonaly, G. J. Koomen, M. Hooper, H. Galone, G. Schepers, E. De Clercg, F. A. W. Koeman, J. P. Kamerlina, J. P. Kamerling, S. Tounson, P. Claes, Hugo Vanden Bossche, G. Bram, J. Marchand-Brynaert, S. Labidalle, J. F. G. Vlieqenthart, R. Pauwels, E. De Vos, M. Baba, R. A. Dommisse, Carl H. Schwabe, Jaap Wilting, Georges J. Hoornaert, F. R. Opperdoes, F. Verberckmoes, H. Schellekens, J. A. Liepoivre, B. H. M. Mruthyunjayasuamy, W. G. J. Hol, Fred R. Opperdoes, J. Osuku Opio, A. F. M. Verheul, J. Cntto, N. De Meyer, L. Mishra, Octaaf J.M. Bos, D. Vanden Berghe, H. Snippe, Lambert H.M. Janssen, D. Van Der Taelen, Ashty Saleh, Ei. Esmans, E. L. Esmans, Frans Compernolle, Isabelle Coppens, J. L. Monal, M. Miocque, F. C. Alderweireldt, A. Jakobs, T. M. Slaghek, P. Joos, S. P. Hiremath, J. Balzarini, M. Renson, P. Herdewi in, Eugene L.M. Vansterkenburg, W. Van Dongen, A. Haemers, H. K. Pandey, L. Plaum, M. J. Wanner, A. Van Aerschot, J. A. Lepoivre, M. Q. Zhang, A. J. Vlietinck, H. Galons, N. Damianos, E. De Clercq, I. Nasri, V. Loppinet
Publikováno v:
Pharmaceutisch Weekblad. 11:C3-C9
s of papers Symposium "New therapeutic developments in human infectious diseases" Organized by the Division Medicinal Chemistry of the Royal Dutch Chemistry Society (Sectie Farmacochemie van de Koninklijke Nederlandse Chemische Vereniging) and the Co
Publikováno v:
Journal of Chromatography B: Biomedical Sciences and Applications. 424:13-21
For a thorough investigation of the drug-binding behaviour and other physicochemical properties of human serum albumin, one needs large amounts of specific fragments of albumin. Such fragments were obtained by careful proteolysis of the native protei
Publikováno v:
Journal of Biological Chemistry. 264:953-959
In order to obtain a better understanding of the neutral-to-base (N-B) transition of human serum albumin, we performed acid/base titration experiments and 500-MHz 1H NMR experiments on albumin and on a large peptic (residues 1–387) and large trypti
Autor:
C. A. M. Van Ginneken, P. P. Kelder, W. Soudijn, A. Bast, Pieter G. Tepper, J. G. van Gelderen, A. R. Goeptar, J. Wilting, R. van de Straat, H. P. Voss, Lambert H.M. Janssen, P. J. M. Van Galen, S. P. A. Boom, R. M. Vromans, F. J. van Bussel, P. A. v. d. Wouw, W. Möller, J. N. L. Go. R. Leurs, N. P. E. Vermeulen, A. J. G. van Zwam, M. A. H. de Zwart, D. de Kaste, Jan Van der Weide, Aziz Bakri, E. Rekka, G. Damsma, J. B. De Vries, K. J. Lusthof, N. P. E. Vermeiden, G. R. M. M. Haenen, E. L. M. van Sterkenburg, Arijan J. Porsius, P. H. G. M. Willems, E. Mutschler, Octaaf J.M. Bos, J. J. H. H. M. de Pont, J. G. C. Van Amsterdam, J. Wemer, C. Llorens-Cortes, N. Rettenmayr, Lambert H. M. Janssen, W. Vleeming, H. L. M. Siero, G. J. Sterk, J. F. Rodriques de Miranda, H. Timmerman, F. B. Pruijn, J. G. Koper, H. W. Th. van Viijmen, J. Dijk, M. C. A. W. Kuit, H. Van der Goot, J. A. Grimbergen, Frans G. M. Russel, M. J. Plug, H. H. v. Rooij, H. Tendijck, M. Groeneveld, F. J. Bosker, K. Kramer, As Horn, Ad P. IJzerman, Bhc Westerink, G. Lambrecht, A. B. Horn, J. F. Rodrigues De Miranda, Marcel J.E. Fischer, P. Tepper, Jaap Wilting, N. J. de Mol, H. W. Th. van Vlijmen, F. J. J. Leusen, M. Veerman
Publikováno v:
Pharmaceutisch Weekblad. 9:338-345
Publikováno v:
Biochemical Pharmacology. 38:1979-1984
In order to obtain information about the kinetics of the process by which warfarin binds to human serum albumin at a molecular level, we performed stopped-flow kinetic experiments on albumin and on a large peptic fragment (residues 1–387) and a lar
Publikováno v:
Biochemical Pharmacology. 37:3905-3909
The warfarin binding behaviour of a large tryptic fragment (residues 198–585 which comprise domains two and three) and of a large peptic fragment (residues 1–387 which comprise domains one and two) of human serum albumin has been studied by circu